ID A0A024UMW1_9STRA Unreviewed; 623 AA.
AC A0A024UMW1;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=Glycerol-3-phosphate dehydrogenase {ECO:0000256|ARBA:ARBA00013029, ECO:0000256|RuleBase:RU361217};
DE EC=1.1.5.3 {ECO:0000256|ARBA:ARBA00013029, ECO:0000256|RuleBase:RU361217};
GN ORFNames=H310_03035 {ECO:0000313|EMBL:ETW06923.1};
OS Aphanomyces invadans.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Aphanomyces.
OX NCBI_TaxID=157072 {ECO:0000313|EMBL:ETW06923.1};
RN [1] {ECO:0000313|EMBL:ETW06923.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NJM9701 {ECO:0000313|EMBL:ETW06923.1};
RG The Broad Institute Genomics Platform;
RA Russ C., Tyler B., van West P., Dieguez-Uribeondo J., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L., Chapman S.B.,
RA Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C., Pearson M.,
RA Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Aphanomyces invadans NJM9701.";
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a quinone + sn-glycerol 3-phosphate = a quinol +
CC dihydroxyacetone phosphate; Xref=Rhea:RHEA:18977, ChEBI:CHEBI:24646,
CC ChEBI:CHEBI:57597, ChEBI:CHEBI:57642, ChEBI:CHEBI:132124; EC=1.1.5.3;
CC Evidence={ECO:0000256|RuleBase:RU361217};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|RuleBase:RU361217};
CC -!- SIMILARITY: Belongs to the FAD-dependent glycerol-3-phosphate
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00007330,
CC ECO:0000256|RuleBase:RU361217}.
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DR EMBL; KI913955; ETW06923.1; -; Genomic_DNA.
DR RefSeq; XP_008864998.1; XM_008866776.1.
DR AlphaFoldDB; A0A024UMW1; -.
DR STRING; 157072.A0A024UMW1; -.
DR EnsemblFungi; H310_03035-t26_1; H310_03035-t26_1-p1; H310_03035.
DR EnsemblProtists; ETW06923; ETW06923; H310_03035.
DR GeneID; 20080085; -.
DR VEuPathDB; FungiDB:H310_03035; -.
DR eggNOG; KOG0042; Eukaryota.
DR OrthoDB; 989271at2759; -.
DR GO; GO:0009331; C:glycerol-3-phosphate dehydrogenase complex; IEA:UniProtKB-UniRule.
DR GO; GO:0004368; F:glycerol-3-phosphate dehydrogenase (quinone) activity; IEA:UniProtKB-EC.
DR GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.8.870; Alpha-glycerophosphate oxidase, cap domain; 1.
DR Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR031656; DAO_C.
DR InterPro; IPR038299; DAO_C_sf.
DR InterPro; IPR006076; FAD-dep_OxRdtase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR000447; G3P_DH_FAD-dep.
DR PANTHER; PTHR11985; GLYCEROL-3-PHOSPHATE DEHYDROGENASE; 1.
DR PANTHER; PTHR11985:SF15; GLYCEROL-3-PHOSPHATE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR Pfam; PF01266; DAO; 1.
DR Pfam; PF16901; DAO_C; 1.
DR PRINTS; PR01001; FADG3PDH.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR PROSITE; PS00977; FAD_G3PDH_1; 1.
DR PROSITE; PS00978; FAD_G3PDH_2; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU361217};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU361217}.
FT DOMAIN 83..414
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 470..605
FT /note="Alpha-glycerophosphate oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16901"
SQ SEQUENCE 623 AA; 69359 MW; EE7C129DF653679E CRC64;
MYRLASPLHR RVAVSLLGAT AGTYSTTSNK STVYHPDSHN KDKNGVFKYV KPIECDDGHV
IVPWEVPDRE LQLQKLKAKD SFDVVVIGGG ATGAGCALDA ATRGMKVALV ERSDFGAGTS
GRSTKLIHGG IRYLETAFMK LDIAAYKLVL EALEERKHML AAAPYMNRAL PIMIPIYTWS
EIPYMWVGAK MYDFVAGHGR SVPGSYYIDS DEAMYQYPNL KKDGLKGAIV YYDGQMNDTR
MNLSLVLTAV QSGATAANYV QVQRLLKDND GNVCGVHVQD THTGEQWDIH ARAVINATGP
FTDDIRLMDN PDADKICVPA AGVHVVLPDH FSPNRMGLII PKTTDGRVLF YLPWENGTLA
GTTDSESAIT MLPSPTKAEV QFILNESNRY LNATVTEADV RSSWSGIRPL VKDPRHPTNT
SQISREHVLD VSPSKMVTIA GGKWTTYRRM AQDTIDKVQA LFPDLAQDAC KTRMMQLVGA
DRIGEVCSQK FDRITITLRE KYHMDKDIAE HLTKNYGTRA LQLGELEKCG FLHRKAGDHP
KRLHPKYPYV ESEVIFAVQQ EYAVRAVDVL ARRTRLAYID AVATEQVMDK VIAMMAQLLK
WDKKRCAAEK DEALAFLATM HTK
//
